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Database: UniProt
Entry: A0A0A2DT90_9PORP
LinkDB: A0A0A2DT90_9PORP
Original site: A0A0A2DT90_9PORP 
ID   A0A0A2DT90_9PORP        Unreviewed;       888 AA.
AC   A0A0A2DT90;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=DNA topoisomerase IV subunit A {ECO:0000313|EMBL:KGN67489.1};
GN   ORFNames=JT26_09730 {ECO:0000313|EMBL:KGN67489.1};
OS   Porphyromonas sp. COT-108 OH1349.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=1537504 {ECO:0000313|EMBL:KGN67489.1, ECO:0000313|Proteomes:UP000030126};
RN   [1] {ECO:0000313|EMBL:KGN67489.1, ECO:0000313|Proteomes:UP000030126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-108 OH1349 {ECO:0000313|Proteomes:UP000030126};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA   Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT   "Porphyromonas sp. COT-108_OH1349 Genome sequencing.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|ARBA:ARBA00008263}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGN67489.1}.
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DR   EMBL; JRAH01000034; KGN67489.1; -; Genomic_DNA.
DR   RefSeq; WP_036849008.1; NZ_JRAH01000034.1.
DR   AlphaFoldDB; A0A0A2DT90; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000030126; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KGN67489.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030126};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          33..461
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          838..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   888 AA;  101612 MW;  D1B4FDA9EA016129 CRC64;
     MSSIEIEEYT EHPDEPQRVS SSGSTYVLTG MYKSWFVNYA SYVILERAVP HIADGLKPVQ
     RRILYTMSQM DDRLIKVANI VGFSMQLHPH GDASISDALV QLGQKDILIQ CQGNWGNILT
     GDGAAAARYI EARLTPFAKE VLFSPKITEY RPSYDGANKE PVRLPVKFPL LLAQGVEGIA
     VGLSSKILPH NVSEILQACV SHLKGETFRL YPDFQTGGHI DVSKYNDGER GGNVKVRANI
     IKKDSKTLVI DELPFGKTTS SLIDSILKAN ERGKIRIRKV DDKTSEKANI EIQLAPGTSS
     DKTIDALYAF TDCEISISPN CCVIKDDKPV FVSVSDVLKD NVERTKNHLH AELQVEYDEL
     REKHLFAYLE QLFIKKRVYK DKKFEEAKST EEAVAYIRTA LAKELKDLVR PVTDEDLRRL
     LEIRMARILR FNEEKNQILL ESLLKEMELA QYRMDHIVEH TIEWYSSLLE KYGAKYPRRT
     KVRSFDTIEA SKVVEKNEKL YVNRQEGFIG TALKKDEFVC NISDIDDIIV FFKDARYIIT
     KVAEKAFVGK DIIHVARFVK NDKRTVYNTI HREGKHGHYF IKRFSVTSFM RDRDYPVGYG
     GEGSKFVYFS ANPNGEAETV RVVLKPKPNQ RQLVFEKDFS SIRIMGRSSR GYLLTKGDVH
     KIVLKQKGVS TLGGRMVWFD HDVNRINYDE RGAFLGEFFP EDKILVIRQN GETYTTSFSD
     TNHFENDIFI IEKYDPNKVW TLIYFDSEQG YTYIKRFQVE DSAKRENILG DGCEMITLSD
     EPYPLFEVSF KGKDQHRLPI VIDVEEYIAV KGIRAKGKRL STFEVGDIEE KEGRKVEVAT
     EDEEVLSLED SPSDDNEEFM ETNRLLGEAT GMKSIPFGNE TEEMEVEE
//
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